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M Kitabatake

Publications and source records attributed to M Kitabatake.

At least 37 records · Page 2Linked to original sources
PubMed1987

Significant increase of urinary low-sulfated heparan-sulfate-related protein in patients with severe systemic scleroderma.

Radioimmunoassay with an antibody produced against urinary low-sulfated heparan-sulfate-related protein was devised and used to screen the heparan sulfate level in the urine of patients with systemic scleroderma. Patients with diffuse scleroderma, and patients also showing polymyositis/dermatomyositis had elevated values, whereas the value in patients with acrosclerotic scleroderma did not differ from that of the control population. In addition, an increase in this protein was associated with the positivity of anti-Scl-70 antibody. These findings suggest an important role for low-sulfated heparan sulfate in the pathobiology of severe systemic scleroderma.

Adult↗
PubMed1987

Increased activity of oligo-2',5'-adenylate synthetase in Down's syndrome and epilepsy.

The level of oligo-2',5'-adenylate synthetase activity is a good marker for the response of cells to interferon. This enzyme can polymerize ATP to form oligonucleotides in the presence of double-stranded RNA, i.e. polyinosinate-cytidylate in vitro. The activity of this enzyme in peripheral blood mononuclear leucocytes was significantly increased in Down's syndrome (P less than 0.01) and epilepsy (P less than 0.01) compared with that in healthy controls, but the increase of activity was not significant in multi-infarct dementia (MID) (P greater than 0.05). Although the patients with Down's syndrome showed higher levels of this enzyme activity than the controls, interferon activity was never detected in the circulation. In addition, the serum of patients with Down's syndrome lacked the capacity to induce this enzyme in NC-37 and FL cells, and furthermore it was shown that the inhibitor of interferon activity was not found in the serum of patients. This discrepancy in Down's syndrome may be the result of the hypersensitivity of cells to interferon. On the contrary, interferon activity (32 IU/ml) was detectable in the circulation of one patient with epilepsy, and the serum of this patient had the capacity to induce this enzyme in NC-37 and FL cells.

2',5'-Oligoadenylate Synthetase↗
PubMed1983

Biotransformation of nitric oxide, nitrite and nitrate.

Biotransformation of NO, nitrite and nitrate was investigated in rats and mice in a 15NO inhalation experiment and intraperitoneal injection experiments of 15N-nitrite and 15N-nitrate, and the following results were obtained: (1) Rats were forced to inhale 15NO (145 ppm, 123 minutes) or were given an intraperitoneal injection of 15N-nitrite (2 mg animal-1 as 15N) or 15N-nitrate (2mg animal-1 as 15N), and determination of 15N recovery in urine was made up to 48 h later. The results were 55, 53 and 78% of the inhaled or injected 15N, respectively. (2) 15N-nitrate in the urine was converted into a 6-nitro derivative of 3,4-xylenol and its identification and quantitative determination were made by the GC-MS method. As to 15N-urea in the urine, identification and quantitative determination were made by the urease method. 15N was present in the urine of rats after 15NO inhalation in the form of NO3- and urea. 75 and 24% respectively. In the urine of rats injected with 15N-nitrite, about 20% of unidentified 15N-compounds not discovered in the inhalation experiment was found. The content of 15N-urea in the urine after injection with 15N-nitrate was lower than that after injection with 15N-nitrite. (3) When 15N-nitrite (0.617 mg animal-1 as 15N) was injected intraperitoneally in mice, 60.7, 7.8 and 0.3% of the injected 15N were found in the urine, feces and exhaled gas (NO, NO2 and NH3 in the gas were caught) up to 48 h after injection respectively, and 1.6% was found in the body 48 h after injection, but the remaining 30% of 15N could not be recovered.

Animals↗
PubMed1983

Immunohistochemical demonstration of proteoglycans in the skin of patients with systemic sclerosis.

Skin proteoglycan was demonstrated by an immunofluorescent technique using an antibody against bovine cartilage proteoglycan, after the cross-reactivity of human proteoglycan with the antiserum had been confirmed. Normal skin exhibited specific fluorescence mainly in the blood vessels as well as in the subepidermal area. The clinically uninvolved skin of systemic sclerosis (SS) revealed no features different from those of normal skin. However, the vascular proteoglycan deposition of early systemic sclerosis was later replaced by deposition between the collagen fibres, which appeared to progress centrifugally in parallel to the increase in the skin sclerosis, suggesting a vascular initiation of the skin lesion. Sclerotic skin was characterized by random deposition between the collagen fibres. Immunoelectron microscopic studies suggested that the random proteoglycan deposition reflected uncontrolled local accumulation of proteoglycan in the interfibrillar matrix around irregularly arranged collagen fibrils.

Adult↗
PubMed1980

Detection of sclerosis-inducing glycosaminoglycan in the skin of an amine-induced experimental skin sclerosis.

The presence of sclerosis-inducing glycosaminoglycan in the skin was confirmed in an experimental skin sclerosis induced by a chemical compound. An experimental skin sclerosis was first produced in the mouse with bis(4-amino-3-methylcyclohexyl)methane. Out of glycosaminoglycans isolated from the slightly changed skin of this experimental skin sclerosis, the one having a heparan sulfate-like structure was able to again induce sclerotic skin changes in another mouse. The chemical composition of this sclerosis-inducing glycosaminoglycan was somewhat similar to that of the scleroderma-inducing glycosaminoglycan isolated previously from the urine of patients with systemic scleroderma.

Animals↗
PubMed1978

Scleroderma-inducing glycosaminoglycan in the urine of patients with systemic scleroderma.

A glycosaminoglycan with scleroderma-inducing effect was isolated and partially purified from the urine of patients with systemic scleroderma. The glycosaminoglycan was an N-sulfated glycosaminoglycuronan and its high total sulfate and 2,5-anhydromannose contents suggest that the glycosaminoglycan is a degradation product of heparin or polysulfated heparin sulfate. Furthermore, the composition of the above glycosaminoglycan was similar to that of the N-sulfated glycosaminoglycan which we observed previously in uninvolved skin of scleroderma.

Adult↗